Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide

H. Shiraga; D. Stallwood; M. Ebadi; R. Pfeiffer; D. Landers; S. Paul

doi:10.1042/bj3000901

Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide

H. Shiraga, D. Stallwood, M. Ebadi, R. Pfeiffer, D. Landers, S. Paul

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin[¹²⁵I-Tyr¹⁰]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.

Original language	English (US)
Pages (from-to)	901-905
Number of pages	5
Journal	Biochemical Journal
Volume	300
Issue number	3
DOIs	https://doi.org/10.1042/bj3000901
State	Published - 1994
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide",

abstract = "In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.",

author = "H. Shiraga and D. Stallwood and M. Ebadi and R. Pfeiffer and D. Landers and S. Paul",

year = "1994",

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T1 - Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide

AU - Shiraga, H.

AU - Stallwood, D.

AU - Ebadi, M.

AU - Pfeiffer, R.

AU - Landers, D.

AU - Paul, S.

PY - 1994

Y1 - 1994

N2 - In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.

AB - In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity, the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.

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Inhibition of calmodulin-dependent myosin light chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide

Abstract

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